P00909 (TRPC_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tryptophan biosynthesis protein TrpCF

Including the following 2 domains:

1. Indole-3-glycerol phosphate synthase
   Short name=IGPS
   EC=4.1.1.48
2. N-(5'-phospho-ribosyl)anthranilate isomerase
   Short name=PRAI
   EC=5.3.1.24

Gene names

Name:	trpC
Ordered Locus Names:	b1262, JW1254

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	452 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Bifunctional enzyme that catalyzes two sequential steps of tryptophan biosynthetic pathway. The first reaction is catalyzed by the isomerase, coded by the TrpF domain; the second reaction is catalyzed by the synthase, coded by the TrpC domain. HAMAP-Rule MF_00134_B
Catalytic activity	N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate. HAMAP-Rule MF_00134_B 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate = 1-C-(3-indolyl)-glycerol 3-phosphate + CO2 + H2O. HAMAP-Rule MF_00134_B
Pathway	Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5. HAMAP-Rule MF_00134_B Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 4/5.
Subunit structure	Monomer.
Sequence similarities	In the N-terminal section; belongs to the TrpC family. In the C-terminal section; belongs to the TrpF family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Aromatic amino acid biosynthesis Tryptophan biosynthesis
Molecular function	Decarboxylase Isomerase Lyase
Technical term	3D-structure Complete proteome Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological_process	tryptophan biosynthetic process Inferred from mutant phenotype PubMed 4865047. Source: EcoCyc
Molecular_function	indole-3-glycerol-phosphate synthase activity Inferred from direct assay PubMed 5332729. Source: EcoCyc phosphoribosylanthranilate isomerase activity Inferred from direct assay PubMed 4865047PubMed 7727401. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 452

452

Tryptophan biosynthesis protein TrpCF HAMAP-Rule MF_00134_B

PRO_0000154277

Regions

Region

1 – 256

256

Indole-3-glycerol phosphate synthase HAMAP-Rule MF_00134_B

Region

257 – 452

196

N-(5'-phosphoribosyl)anthranilate isomerase HAMAP-Rule MF_00134_B

Experimental info

Sequence conflict

30

1

Missing in CAA23673. Ref.3

Sequence conflict

94

1

Q → R in CAA23664. Ref.1

Sequence conflict

94

1

Q → R in AAA57299. Ref.1

Sequence conflict

94

1

Q → R in CAA23673. Ref.3

Sequence conflict

284

1

Missing in CAA23673. Ref.3

Sequence conflict

293

1

V → D in CAA23673. Ref.3

Sequence conflict

329

1

A → V in CAA23664. Ref.1

Sequence conflict

329

1

A → V in AAA57299. Ref.1

Sequence conflict

329

1

A → V in CAA23673. Ref.3

Sequence conflict

398

1

S → T in CAA23664. Ref.1

Sequence conflict

398

1

S → T in AAA57299. Ref.1

Sequence conflict

398

1

S → T in CAA23673. Ref.3

Sequence conflict

398

1

S → T in AAB60033. Ref.4

Secondary structure

1

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452

Helix Strand Turn

Details...

Helix

4 – 22

19

Helix

25 – 27

3

Helix

29 – 31

3

Helix

39 – 43

5

Beta strand

45 – 47

3

Beta strand

49 – 54

6

Beta strand

56 – 58

3

Turn

59 – 61

3

Beta strand

62 – 64

3

Helix

70 – 77

8

Turn

78 – 80

3

Beta strand

82 – 87

6

Turn

91 – 93

3

Helix

99 – 106

8

Beta strand

111 – 115

5

Helix

120 – 128

9

Beta strand

132 – 137

6

Turn

138 – 140

3

Helix

143 – 155

13

Beta strand

159 – 164

6

Helix

167 – 175

9

Beta strand

179 – 186

8

Turn

188 – 190

3

Helix

196 – 205

10

Beta strand

209 – 215

7

Helix

220 – 226

7

Turn

227 – 229

3

Beta strand

231 – 235

5

Helix

237 – 240

4

Helix

245 – 254

10

Helix

265 – 274

10

Beta strand

277 – 282

6

Helix

293 – 302

10

Beta strand

306 – 313

8

Helix

316 – 326

11

Beta strand

329 – 333

5

Helix

335 – 337

3

Helix

339 – 348

10

Beta strand

353 – 360

8

Beta strand

362 – 364

3

Beta strand

375 – 380

6

Helix

391 – 394

4

Beta strand

402 – 407

6

Turn

410 – 412

3

Helix

413 – 417

5

Beta strand

422 – 426

5

Helix

428 – 430

3

Beta strand

431 – 433

3

Helix

439 – 450

12

Sequences

	Sequence		Length	Mass (Da)
	P00909 [UniParc]. Last modified August 29, 2003. Version 3. Checksum: AEAE60B25E61E8A8	FASTA	452	49,361
	10 20 30 40 50 60 MQTVLAKIVA DKAIWVEARK QQQPLASFQN EVQPSTRHFY DALQGARTAF ILECKKASPS 70 80 90 100 110 120 KGVIRDDFDP ARIAAIYKHY ASAISVLTDE KYFQGSFNFL PIVSQIAPQP ILCKDFIIDP 130 140 150 160 170 180 YQIYLARYYQ ADACLLMLSV LDDDQYRQLA AVAHSLEMGV LTEVSNEEEQ ERAIALGAKV 190 200 210 220 230 240 VGINNRDLRD LSIDLNRTRE LAPKLGHNVT VISESGINTY AQVRELSHFA NGFLIGSALM 250 260 270 280 290 300 AHDDLHAAVR RVLLGENKVC GLTRGQDAKA AYDAGAIYGG LIFVATSPRC VNVEQAQEVM 310 320 330 340 350 360 AAAPLQYVGV FRNHDIADVV DKAKVLSLAA VQLHGNEEQL YIDTLREALP AHVAIWKALS 370 380 390 400 410 420 VGETLPAREF QHVDKYVLDN GQGGSGQRFD WSLLNGQSLG NVLLAGGLGA DNCVEAAQTG 430 440 450 CAGLDFNSAV ESQPGIKDAR LLASVFQTLR AY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Gene structure in the tryptophan operon of Escherichia coli. Nucleotide sequence of trpC and the flanking intercistronic regions." Christie G.E., Platt T. J. Mol. Biol. 142:519-530(1980) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Nucleotide sequence of the trpD and trpC genes of Salmonella typhimurium." Horowitz H., van Arsdell J., Platt T. J. Mol. Biol. 169:775-797(1983) [PubMed] [Europe PMC] [Abstract] Cited for: SEQUENCE REVISION TO 94 AND 398.
[3]	"The complete nucleotide sequence of the tryptophan operon of Escherichia coli." Yanofsky C., Platt T., Crawford I.P., Nichols B.P., Christie G.E., Horowitz H., van Cleemput M., Wu A.M. Nucleic Acids Res. 9:6647-6668(1981) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"Molecular evolution of the Escherichia coli chromosome. IV. Sequence comparisons." Milkman R., Bridges M.M. Genetics 133:455-468(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map." Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K. , Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T. DNA Res. 3:363-377(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[7]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[8]	"Escherichia coli proteome analysis using the gene-protein database." VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C. Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY 2D-GEL.
[9]	"Three-dimensional structure of the bifunctional enzyme phosphoribosylanthranilate isomerase: indoleglycerolphosphate synthase from Escherichia coli refined at 2.0-A resolution." Wilmanns M., Priestle J.P., Niermann T., Jansonius J.N. J. Mol. Biol. 223:477-507(1992) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), SEQUENCE REVISION TO 319.
[10]	"Crystallization and structure solution at 4-A resolution of the recombinant synthase domain of N-(5'-phosphoribosyl)anthranilate isomerase:indole-3-glycerol-phosphate synthase from Escherichia coli complexed to a substrate analogue." Wilmanns M., Schlagenhauf E., Fol B., Jansonius J.N. Protein Eng. 3:173-180(1990) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS) OF 257-452.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

V00366 Genomic DNA. Translation: CAA23664.1.
V00372 Genomic DNA. Translation: CAA23673.1.
J01714 Genomic DNA. Translation: AAA57299.1.
U23489 Genomic DNA. Translation: AAB60033.1.
U00096 Genomic DNA. Translation: AAC74344.2.
AP009048 Genomic DNA. Translation: BAA14794.1.

PIR

GWEC. A64874.

RefSeq

NP_415778.2. NC_000913.2.
YP_489530.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1JCM	X-ray	2.10	P	1-259	[»]
1PII	X-ray	2.00	A	1-452	[»]
2KZH	NMR	-	A	255-384	[»]

ProteinModelPortal

P00909.

SMR

P00909. Positions 1-452.

ModBase

Search...

Protein-protein interaction databases

IntAct

P00909. 2 interactions.

STRING

511145.b1262.

Proteomic databases

PaxDb

P00909.

PRIDE

P00909.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC74344; AAC74344; b1262.
BAA14794; BAA14794; BAA14794.

GeneID

12931128.
945519.

KEGG

ecj:Y75_p1236.
eco:b1262.

PATRIC

32117784. VBIEscCol129921_1312.

Organism-specific databases

EchoBASE

EB1019.

EcoGene

EG11026. trpC.

Phylogenomic databases

eggNOG

COG0134.

HOGENOM

HOG000280458.

KO

K13498.

OMA

YILECKK.

ProtClustDB

PRK09427.

Enzyme and pathway databases

BioCyc

EcoCyc:PRAI-IGPS.
ECOL316407:JW1254-MONOMER.
MetaCyc:PRAI-IGPS.

UniPathway

UPA00035; UER00042.
UPA00035; UER00043.

Gene expression databases

Genevestigator

P00909.

Family and domain databases

Gene3D

3.20.20.70. 2 hits.

HAMAP

MF_00134_B. IGPS_B. Fused.
MF_00135. PRAI. Fused.

InterPro

IPR013785. Aldolase_TIM.
IPR013798. Indole-3-glycerol_P_synth.
IPR001468. Indole-3-GlycerolPSynthase_CS.
IPR001240. PRAI_dom.
IPR011060. RibuloseP-bd_barrel.
[Graphical view]

Pfam

PF00218. IGPS. 1 hit.
PF00697. PRAI. 1 hit.
[Graphical view]

SUPFAM

SSF51366. RibP_bind_barrel. 2 hits.

PROSITE

PS00614. IGPS. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P00909.

Entry information

Entry name

TRPC_ECOLI

Accession

Primary (citable) accession number: P00909
Secondary accession number(s): P78059, P78234, P94704

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	August 29, 2003
Last modified:	May 29, 2013
This is version 133 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program